Results 51 to 60 of about 72,088 (314)

Literature-based discovery of diabetes- and ROS-related targets [PDF]

, 2010
Background Reactive oxygen species (ROS) are known mediators of cellular damage in multiple diseases including diabetic complications. Despite its importance, no comprehensive database is currently available for the genes associated with ROS.
A Erol, A Fontayne, A Iaccio, Adam D Schuyler, AG Reaume, AM Vincent, AM Vincent, AM Vincent, AM Vincent, American-Diabetes-Association, BJ Turner, C Figueroa-Romero, C Plake, D Rebholz-Schuhmann, David J States, E Schwedhelm, EH Sarsour, EL Feldman, EM Olofsson, Eva L Feldman, F Folli, FA Hakim, FR DeRubertis, H Ilieva, H V Jagadish, HB Lee, I Vastrik, J Hur, JL Edwards, JM Jimenez-Andrade, JS Pan, Junguk Hur, JW Russell, KA Sullivan, Kelli A Sullivan, KK Ohlemiller, L Hirschman, M Ashburner, M Brownlee, M Fukuda, M Fukuda, M Kanehisa, M Kawase, Manjusha Pande, N Kameyama, PJ Shaw, RA Fisher, S Cetinkalp, S Ghosh, T Matsunami, VI Perez, Y Aliciguzel, Y Benjamini, Yu Hong, Z Bagi   +54 more
core   +5 more sources

Oxidized SOD1 alters proteasome activities in vitro and in the cortex of SOD1 overexpressing mice

FEBS Letters, 2005
Premature ageing, one of the characteristics of Down syndrome (DS), may involve oxidative stress and impairment of proteasome activity. Transgenic mice overexpressing the human copper/zinc superoxide dismutase (SOD1) gene are one of the first murine models for DS and it has been shown that SOD1 overexpression might be either deleterious or beneficial ...
Emmanuel Bourdon, Bertrand Friguet, Marie Le Pecheur, Evelyne Paly, Jacqueline London, Luc Farout   +5 more
openaire   +3 more sources

SOD1 Is Essential for the Viability of DT40 Cells and Nuclear SOD1 Functions as a Guardian of Genomic DNA [PDF]

Journal of Nucleic Acids, 2010
Reactive oxygen species (ROSs) are produced during normal cellular metabolism, particularly by respiration in mitochondria, and these ROSs are considered to cause oxidative damage to macromolecules, including DNA. In our previous paper, we found no indication that depletion of mitochondrial superoxide dismutase, SOD2, resulted in an increase in DNA ...
Keizo Tano, Takemi Enomoto, Takemi Enomoto, Masami Watanabe, Shusuke Tada, Hanako Yoshii, Eri Inoue, Jun Nakamura, Masayuki Seki   +8 more
openaire   +3 more sources

Difficulties in diagnosing amyotrophic lateral sclerosis in a HIV-Positive Patient

Журнал инфектологии, 2018
We described a case of amyotrophic lateral sclerosis (ALS) with comorbid HIV infection. The diagnosis was confirmed by genetic tests. The difficulty of the differential diagnosis between amyotrophic lateral sclerosis and HIV-associated ALS syndrome is ...
T. M. Alekseeva, N. V. Skripchenko, S. V. Lobzin, V. S. Demeshonok, E. A. Yurkina, V. D. Nazarov, S. V. Lapin   +6 more
doaj   +1 more source

Tofersen for SOD1 ALS

Neurodegenerative Disease Management
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative condition affecting the motor system. The heterogenous nature of ALS complicates trial design. Genetic forms of ALS present an opportunity to intervene in a less heterogeneous population.
William H Everett, Robert C Bucelli
openaire   +2 more sources

A model for gain of function in superoxide dismutase

Biochemistry and Biophysics Reports, 2020
Studies have found that mutant, misfolded superoxide dismutase [Cu–Zn] (SOD1) can convert wild type SOD1 (wtSOD1) in a prion-like fashion, and that misfolded wtSOD1 can be propagated by release and uptake of protein aggregates. In developing a prion-like
Eamonn F. Healy, Analise Roth-Rodriguez, Santiago Toledo   +2 more
doaj   +1 more source

Folding of Cu, Zn superoxide dismutase and Familial Amyotrophic Lateral Sclerosis [PDF]

, 2003
Cu,Zn superoxide dismutase (SOD1) has been implicated in the familial form of the neurodegenerative disease Amyotrophic Lateral Sclerosis (ALS). It has been suggested that mutant mediated SOD1 misfolding/aggregation is an integral part of the pathology ...
Ding, Feng, Dokholyan, Nikolay V., Khare, Sagar D.   +2 more
core   +4 more sources

Ligand binding and aggregation of pathogenic SOD1 [PDF]

Nature Communications, 2013
Mutations in the gene encoding Cu/Zn superoxide dismutase-1 cause amyotrophic lateral sclerosis. Superoxide dismutase-1 mutations decrease protein stability and promote aggregation. The mutant monomer is thought to be an intermediate in the pathway from the superoxide dismutase-1 dimer to aggregate. Here we find that the monomeric copper-apo, zinc-holo
Gareth S.A. Wright, Svetlana V. Antonyuk, Neil M. Kershaw, Richard W. Strange, S Samar Hasnain   +4 more
openaire   +3 more sources

Association of GPX1 Pro198Leu and SOD1 A251G polymorphisms with risk of acute kidney rejection [PDF]

Scripta Medica
Background/Aim: Acute rejection is one factor threatening the success of kidney transplantation. One of the factors that can cause graft rejection is oxidative stress.
Rayatpisheh Shima, Karimi Mohammad-Hossein, Saadat Iraj   +2 more
doaj   +1 more source

Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase. [PDF]

PLoS ONE, 2009
Mutations in the gene encoding Cu-Zn superoxide dismutase (SOD1) are one of the causes of familial amyotrophic lateral sclerosis (FALS). Fibrillar inclusions containing SOD1 and SOD1 inclusions that bind the amyloid-specific dye thioflavin S have been ...
Zeynep A Oztug Durer, Jeffrey A Cohlberg, Phong Dinh, Shelby Padua, Krista Ehrenclou, Sean Downes, James K Tan, Yoko Nakano, Christopher J Bowman, Jessica L Hoskins, Chuhee Kwon, Andrew Z Mason, Jorge A Rodriguez, Peter A Doucette, Bryan F Shaw, Joan Selverstone Valentine   +15 more
doaj   +1 more source